|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
1-437 |
0e+00 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 942.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 1 MTANNLREQISQLVAQYANEALSPKPFVAGTSVVPPSGKVIGAKELQLMVEASLDGWLTTGRFNDAFEKKLGEFIGVPHV 80
Cdd:PRK15407 2 MTEEELRQQILELVREYAELAHAPKPFVPGKSPIPPSGKVIDAKELQNLVDASLDFWLTTGRFNDAFEKKLAEFLGVRYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 81 LTTTSGSSANLLALTALTSPKLGERALKPGDEVITVAAGFPTTVNPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSK 160
Cdd:PRK15407 82 LLVNSGSSANLLAFSALTSPKLGDRALKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 161 AIMIAHTLGNAFNLSEVRRIADKYNLWLIEDCCDALGTTYEGQMVGTFGDIGTVSFYPAHHITMGEGGAVFTKSGELKKI 240
Cdd:PRK15407 162 AIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPLLKKI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 241 IESFRDWGRDCYCAPGCDNTCGKRFGQQLGSLPQGYDHKYTYSHLGYNLKITDMQAACGLAQLERVEEFVEQRKANFSYL 320
Cdd:PRK15407 242 IESFRDWGRDCWCAPGCDNTCGKRFGWQLGELPFGYDHKYTYSHLGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 321 KQGLQSCTEFLELPEATEKSDPSWFGFPITLKETSGVNRVELVKFLDEAKIGTRLLFAGNLIRQPYFANVKYRVVGELTN 400
Cdd:PRK15407 322 KEGLASLEDFLILPEATPNSDPSWFGFPITVKEDAGFTRVELVKYLEENKIGTRLLFAGNLTRQPYFKGVKYRVVGELTN 401
|
410 420 430
....*....|....*....|....*....|....*..
gi 1137344229 401 TDRIMNQTFWIGIYPGLTTEHLDYVVSKFEEFFGLNF 437
Cdd:PRK15407 402 TDRIMNDTFWIGVYPGLTEEMLDYVIEKIEEFFGLNF 438
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
34-433 |
2.06e-157 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 449.13 E-value: 2.06e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 34 VPPSGKVIGAKELQLMVEASLDGWLTTGRFNDAFEKKLGEFIGVPHVLTTTSGSSANLLALTALTspklgeraLKPGDEV 113
Cdd:COG0399 2 IPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALG--------IGPGDEV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 114 ITVAAGFPTTVNPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMIAHTLGNAFNLSEVRRIADKYNLWLIEDCC 193
Cdd:COG0399 74 ITPAFTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 194 DALGTTYEGQMVGTFGDIGTVSFYPAHHITMGEGGAVFTKSGELKKIIESFRDWGRDcycapgcdntcgkrfgqqlgslp 273
Cdd:COG0399 154 QALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRD----------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 274 qgYDHKYTYSHLGYNLKITDMQAACGLAQLERVEEFVEQRKANFSYLKQGLQSCtEFLELPEATEKSDPSWFGFPITLKE 353
Cdd:COG0399 211 --RDAKYEHVELGYNYRMDELQAAIGLAQLKRLDEFIARRRAIAARYREALADL-PGLTLPKVPPGAEHVYHLYVIRLDE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 354 tsGVNRVELVKFLDEAKIGTRLLFAGNLIRQPYFANVKYRvVGELTNTDRIMNQTFWIGIYPGLTTEHLDYVVSKFEEFF 433
Cdd:COG0399 288 --GEDRDELIAALKARGIGTRVHYPIPLHLQPAYRDLGYR-PGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
40-430 |
3.18e-154 |
|
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.
Pssm-ID: 395827 Cd Length: 360 Bit Score: 440.95 E-value: 3.18e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 40 VIGAKELQLMVEASLD-GWLTTGRFNDAFEKKLGEFIGVPHVLTTTSGSSANLLALTALtspklgerALKPGDEVITVAA 118
Cdd:pfam01041 1 PDIDEEELAAVREVLKsGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRAL--------GVGPGDEVITPSF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 119 GFPTTVNPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMIAHTLGNAFNLSEVRRIADKYNLWLIEDCCDALGT 198
Cdd:pfam01041 73 TFVATANAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 199 TYEGQMVGTFGDIGTVSFYPAHHITMGEGGAVFTKSGELKKIIESFRDWGRDcycapgcdntcgkrfgqqlgslpQGYDH 278
Cdd:pfam01041 153 TYQGKKVGTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMV-----------------------RKADK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 279 KYTYSHLGYNLKITDMQAACGLAQLERVEEFVEQRKANFSYLKQGLQSCTEFLELPEATEKSDPSWFGFPITLKEtSGVN 358
Cdd:pfam01041 210 RYWHEVLGYNYRMTEIQAAIGLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVHAWHLFPILVPE-EAIN 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1137344229 359 RVELVKFLDEAKIGTRLLFAGNLIRQPYFANVKYRVVGELTNTDRIMNQTFWIGIYPGLTTEHLDYVVSKFE 430
Cdd:pfam01041 289 RDELVEALKEAGIGTRVHYPIPLHLQPYYRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
45-430 |
1.44e-143 |
|
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.
Pssm-ID: 99740 [Multi-domain] Cd Length: 352 Bit Score: 413.48 E-value: 1.44e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 45 ELQLMVEASLDGWLTTGRFNDAFEKKLGEFIGVPHVLTTTSGSSANLLALTALTspklgeraLKPGDEVITVAAGFPTTV 124
Cdd:cd00616 1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALG--------IGPGDEVIVPSFTFVATA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 125 NPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMIAHTLGNAFNLSEVRRIADKYNLWLIEDCCDALGTTYEGQM 204
Cdd:cd00616 73 NAILLLGATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 205 VGTFGDIGTVSFYPAHHITMGEGGAVFTKSGELKKIIESFRDWGRDCycapgcdntcgkrfgqqlgslpqgYDHKYTYSH 284
Cdd:cd00616 153 VGTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDR------------------------DRFKYEHEI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 285 LGYNLKITDMQAACGLAQLERVEEFVEQRKANFSYLKQGLQSCtEFLELPEATEKSDPSWFGFPITLKETSGVNRVELVK 364
Cdd:cd00616 209 LGYNYRLSEIQAAIGLAQLEKLDEIIARRREIAERYKELLADL-PGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIE 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137344229 365 FLDEAKIGTRLLFAGNLIRQPYFANVKYRvVGELTNTDRIMNQTFWIGIYPGLTTEHLDYVVSKFE 430
Cdd:cd00616 288 ALKEAGIETRVHYPPLHHQPPYKKLLGYP-PGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| ECA_wecE |
TIGR02379 |
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ... |
35-433 |
1.75e-40 |
|
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of TDP-4-keto-6-deoxy-D-glucose transaminases, the WecE (formerly RffA) protein of enterobacterial common antigen (ECA) biosynthesis, from enterobacteria. It also includes closely matching sequence from species not expected to make ECA, but which contain other genes for the biosynthesis of TDP-4-keto-6-deoxy-D-Glc, an intermediate in the biosynthesis of other compounds as well and the substrate of WecA. This family belongs to the DegT/DnrJ/EryC1/StrS aminotransferase family (pfam01041). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 131432 Cd Length: 376 Bit Score: 148.43 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 35 PPsgkVIGaKELQLMVEASLDGWLT-TGRFNDAFEKKLGEFIGVPHVLTTTSGSSAnlLALTALTSPklgeraLKPGDEV 113
Cdd:TIGR02379 7 PP---VTG-TELDYIQEAISSGKLSgDGPFTRRCEQWLEQRTGTKKALLTPSCTAA--LEMAALLLD------IQPGDEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 114 ITVAAGFPTTVNPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMIAHTLGNAFNLSEVRRIADKYNLWLIEDCC 193
Cdd:TIGR02379 75 IMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 194 DALGTTYEGQMVGTFGDIGTVSFYPAHHITMG-EGGAVFTKSGELKKIIESFRDWGRDcycapgcdntcgkrfgqqLGSL 272
Cdd:TIGR02379 155 QGVMSTYKGRALGSIGHIGTFSFHETKNYTSGgEGGALLINDQAFIERAEIIREKGTN------------------RSQF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 273 PQGYDHKYTYSHLGYNLKITDMQAACGLAQLERVEEFVEQRKANFSYLKQGLQSCTE--FLELPEATEKSDPSWFGFPIT 350
Cdd:TIGR02379 217 FRGEVDKYTWRDIGSSYLPSELQAAYLWAQLEQADRINQQRLALWQNYYDALAPLEEkgIIELPSIPDGCQHNAHMFYIK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 351 LKetSGVNRVELVKFLDEAKIGTRLLFAgNLIRQPyfANVKY-RVVGELTNTDRIMNQTFWIGIYPGLTTEHLDYVVSKF 429
Cdd:TIGR02379 297 LR--DIDDRSELINFLKEQEIMAVFHYI-PLHSSP--AGRHFgRFHGEDIYTTKESERLVRLPLFYGLSPEDQRRVIATL 371
|
....
gi 1137344229 430 EEFF 433
Cdd:TIGR02379 372 CDYL 375
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
1-437 |
0e+00 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 942.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 1 MTANNLREQISQLVAQYANEALSPKPFVAGTSVVPPSGKVIGAKELQLMVEASLDGWLTTGRFNDAFEKKLGEFIGVPHV 80
Cdd:PRK15407 2 MTEEELRQQILELVREYAELAHAPKPFVPGKSPIPPSGKVIDAKELQNLVDASLDFWLTTGRFNDAFEKKLAEFLGVRYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 81 LTTTSGSSANLLALTALTSPKLGERALKPGDEVITVAAGFPTTVNPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSK 160
Cdd:PRK15407 82 LLVNSGSSANLLAFSALTSPKLGDRALKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 161 AIMIAHTLGNAFNLSEVRRIADKYNLWLIEDCCDALGTTYEGQMVGTFGDIGTVSFYPAHHITMGEGGAVFTKSGELKKI 240
Cdd:PRK15407 162 AIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPLLKKI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 241 IESFRDWGRDCYCAPGCDNTCGKRFGQQLGSLPQGYDHKYTYSHLGYNLKITDMQAACGLAQLERVEEFVEQRKANFSYL 320
Cdd:PRK15407 242 IESFRDWGRDCWCAPGCDNTCGKRFGWQLGELPFGYDHKYTYSHLGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 321 KQGLQSCTEFLELPEATEKSDPSWFGFPITLKETSGVNRVELVKFLDEAKIGTRLLFAGNLIRQPYFANVKYRVVGELTN 400
Cdd:PRK15407 322 KEGLASLEDFLILPEATPNSDPSWFGFPITVKEDAGFTRVELVKYLEENKIGTRLLFAGNLTRQPYFKGVKYRVVGELTN 401
|
410 420 430
....*....|....*....|....*....|....*..
gi 1137344229 401 TDRIMNQTFWIGIYPGLTTEHLDYVVSKFEEFFGLNF 437
Cdd:PRK15407 402 TDRIMNDTFWIGVYPGLTEEMLDYVIEKIEEFFGLNF 438
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
34-433 |
2.06e-157 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 449.13 E-value: 2.06e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 34 VPPSGKVIGAKELQLMVEASLDGWLTTGRFNDAFEKKLGEFIGVPHVLTTTSGSSANLLALTALTspklgeraLKPGDEV 113
Cdd:COG0399 2 IPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALG--------IGPGDEV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 114 ITVAAGFPTTVNPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMIAHTLGNAFNLSEVRRIADKYNLWLIEDCC 193
Cdd:COG0399 74 ITPAFTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 194 DALGTTYEGQMVGTFGDIGTVSFYPAHHITMGEGGAVFTKSGELKKIIESFRDWGRDcycapgcdntcgkrfgqqlgslp 273
Cdd:COG0399 154 QALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRD----------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 274 qgYDHKYTYSHLGYNLKITDMQAACGLAQLERVEEFVEQRKANFSYLKQGLQSCtEFLELPEATEKSDPSWFGFPITLKE 353
Cdd:COG0399 211 --RDAKYEHVELGYNYRMDELQAAIGLAQLKRLDEFIARRRAIAARYREALADL-PGLTLPKVPPGAEHVYHLYVIRLDE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 354 tsGVNRVELVKFLDEAKIGTRLLFAGNLIRQPYFANVKYRvVGELTNTDRIMNQTFWIGIYPGLTTEHLDYVVSKFEEFF 433
Cdd:COG0399 288 --GEDRDELIAALKARGIGTRVHYPIPLHLQPAYRDLGYR-PGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
40-430 |
3.18e-154 |
|
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.
Pssm-ID: 395827 Cd Length: 360 Bit Score: 440.95 E-value: 3.18e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 40 VIGAKELQLMVEASLD-GWLTTGRFNDAFEKKLGEFIGVPHVLTTTSGSSANLLALTALtspklgerALKPGDEVITVAA 118
Cdd:pfam01041 1 PDIDEEELAAVREVLKsGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRAL--------GVGPGDEVITPSF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 119 GFPTTVNPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMIAHTLGNAFNLSEVRRIADKYNLWLIEDCCDALGT 198
Cdd:pfam01041 73 TFVATANAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 199 TYEGQMVGTFGDIGTVSFYPAHHITMGEGGAVFTKSGELKKIIESFRDWGRDcycapgcdntcgkrfgqqlgslpQGYDH 278
Cdd:pfam01041 153 TYQGKKVGTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMV-----------------------RKADK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 279 KYTYSHLGYNLKITDMQAACGLAQLERVEEFVEQRKANFSYLKQGLQSCTEFLELPEATEKSDPSWFGFPITLKEtSGVN 358
Cdd:pfam01041 210 RYWHEVLGYNYRMTEIQAAIGLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVHAWHLFPILVPE-EAIN 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1137344229 359 RVELVKFLDEAKIGTRLLFAGNLIRQPYFANVKYRVVGELTNTDRIMNQTFWIGIYPGLTTEHLDYVVSKFE 430
Cdd:pfam01041 289 RDELVEALKEAGIGTRVHYPIPLHLQPYYRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
45-430 |
1.44e-143 |
|
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.
Pssm-ID: 99740 [Multi-domain] Cd Length: 352 Bit Score: 413.48 E-value: 1.44e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 45 ELQLMVEASLDGWLTTGRFNDAFEKKLGEFIGVPHVLTTTSGSSANLLALTALTspklgeraLKPGDEVITVAAGFPTTV 124
Cdd:cd00616 1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALG--------IGPGDEVIVPSFTFVATA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 125 NPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMIAHTLGNAFNLSEVRRIADKYNLWLIEDCCDALGTTYEGQM 204
Cdd:cd00616 73 NAILLLGATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 205 VGTFGDIGTVSFYPAHHITMGEGGAVFTKSGELKKIIESFRDWGRDCycapgcdntcgkrfgqqlgslpqgYDHKYTYSH 284
Cdd:cd00616 153 VGTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDR------------------------DRFKYEHEI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 285 LGYNLKITDMQAACGLAQLERVEEFVEQRKANFSYLKQGLQSCtEFLELPEATEKSDPSWFGFPITLKETSGVNRVELVK 364
Cdd:cd00616 209 LGYNYRLSEIQAAIGLAQLEKLDEIIARRREIAERYKELLADL-PGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIE 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137344229 365 FLDEAKIGTRLLFAGNLIRQPYFANVKYRvVGELTNTDRIMNQTFWIGIYPGLTTEHLDYVVSKFE 430
Cdd:cd00616 288 ALKEAGIETRVHYPPLHHQPPYKKLLGYP-PGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
25-433 |
1.11e-47 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 167.70 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 25 KPFVAGtsvvppsgkvigaKELQLMVEA------SLDGWLTTgRFNDAFEKKLGefigVPHVLTTTSGSSAnlLALTALt 98
Cdd:PRK11706 6 KPPVVG-------------TELDYIQQAmssgklCGDGGFTR-RCQQWLEQRFG----SAKVLLTPSCTAA--LEMAAL- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 99 spkLGEraLKPGDEVITVAAGFPTTVNPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMIAHTLGNAFNLSEVR 178
Cdd:PRK11706 65 ---LLD--IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 179 RIADKYNLWLIEDCCDALGTTYEGQMVGTFGDIGTVSFYPAHHITMGEGGAVFTKSGELKKIIESFRDWGrdcycapgcd 258
Cdd:PRK11706 140 ALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIERAEIIREKG---------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 259 nTCGKRF--GQqlgslpqgYDhKYTYSHLGYNLKITDMQAACGLAQLERVEEFVEQRKANFSYLKQGLQSCTE--FLELP 334
Cdd:PRK11706 210 -TNRSQFfrGQ--------VD-KYTWVDIGSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALAPLAEagRIELP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 335 EATEKSDPSWFGFPITLKETSgvNRVELVKFLDEAKIGTrllfagnlirqpYF---------ANVKY-RVVGELTNTDRI 404
Cdd:PRK11706 280 SIPDDCKHNAHMFYIKLRDLE--DRSALINFLKEAGIMA------------VFhyiplhsspAGERFgRFHGEDRYTTKE 345
|
410 420
....*....|....*....|....*....
gi 1137344229 405 MNQTFWIGIYPGLTTEHLDYVVSKFEEFF 433
Cdd:PRK11706 346 SERLLRLPLFYNLTDVEQRTVIDTILEFF 374
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
35-434 |
1.11e-42 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 154.41 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 35 PPSGKVIGAKELQLMVEASLDGWLTTGRFNDAFEKKLGEFIGVPHVLTTTSGSSANLLALTALtspklgerALKPGDEVI 114
Cdd:PRK11658 6 PFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMAL--------GIGPGDEVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 115 TVAAGFPTTVNPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMIAHTLGNAFNLSEVRRIADKYNLWLIEDCCD 194
Cdd:PRK11658 78 TPSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 195 ALGTTYEGQMVgtfGDIGTV--SFYPAHHITMGEGGAVFTKSGELKKIIES--FRDWGRDCYcapgcDNtcgkrfgQQLG 270
Cdd:PRK11658 158 AVGTYYKGRHI---GARGTAifSFHAIKNITCAEGGLVVTDDDELADRLRSlkFHGLGVDAF-----DR-------QTQG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 271 SLPQ------GYDhkytyshlgYNLkiTDMQAACGLAQLERVEEFVEQRKANFSYLKQGLQScTEFLELPEATEKSDPSW 344
Cdd:PRK11658 223 RAPQaevltpGYK---------YNL--ADINAAIALVQLAKLEALNARRREIAARYLQALAD-LPFQPLSLPAWPHQHAW 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 345 FGFPITL-KETSGVNRVELVKFLDEAKIGTRLLF-AGNLirQPYfanvkYRvvgE------LTNTD----RIMNqtfwIG 412
Cdd:PRK11658 291 HLFIIRVdEERCGISRDALMEALKERGIGTGLHFrAAHT--QKY-----YR---ErfptlsLPNTEwnseRICS----LP 356
|
410 420
....*....|....*....|..
gi 1137344229 413 IYPGLTTEHLDYVVSKFEEFFG 434
Cdd:PRK11658 357 LFPDMTDADVDRVITALQQIAG 378
|
|
| ECA_wecE |
TIGR02379 |
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ... |
35-433 |
1.75e-40 |
|
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of TDP-4-keto-6-deoxy-D-glucose transaminases, the WecE (formerly RffA) protein of enterobacterial common antigen (ECA) biosynthesis, from enterobacteria. It also includes closely matching sequence from species not expected to make ECA, but which contain other genes for the biosynthesis of TDP-4-keto-6-deoxy-D-Glc, an intermediate in the biosynthesis of other compounds as well and the substrate of WecA. This family belongs to the DegT/DnrJ/EryC1/StrS aminotransferase family (pfam01041). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 131432 Cd Length: 376 Bit Score: 148.43 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 35 PPsgkVIGaKELQLMVEASLDGWLT-TGRFNDAFEKKLGEFIGVPHVLTTTSGSSAnlLALTALTSPklgeraLKPGDEV 113
Cdd:TIGR02379 7 PP---VTG-TELDYIQEAISSGKLSgDGPFTRRCEQWLEQRTGTKKALLTPSCTAA--LEMAALLLD------IQPGDEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 114 ITVAAGFPTTVNPAIQNGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMIAHTLGNAFNLSEVRRIADKYNLWLIEDCC 193
Cdd:TIGR02379 75 IMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 194 DALGTTYEGQMVGTFGDIGTVSFYPAHHITMG-EGGAVFTKSGELKKIIESFRDWGRDcycapgcdntcgkrfgqqLGSL 272
Cdd:TIGR02379 155 QGVMSTYKGRALGSIGHIGTFSFHETKNYTSGgEGGALLINDQAFIERAEIIREKGTN------------------RSQF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 273 PQGYDHKYTYSHLGYNLKITDMQAACGLAQLERVEEFVEQRKANFSYLKQGLQSCTE--FLELPEATEKSDPSWFGFPIT 350
Cdd:TIGR02379 217 FRGEVDKYTWRDIGSSYLPSELQAAYLWAQLEQADRINQQRLALWQNYYDALAPLEEkgIIELPSIPDGCQHNAHMFYIK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 351 LKetSGVNRVELVKFLDEAKIGTRLLFAgNLIRQPyfANVKY-RVVGELTNTDRIMNQTFWIGIYPGLTTEHLDYVVSKF 429
Cdd:TIGR02379 297 LR--DIDDRSELINFLKEQEIMAVFHYI-PLHSSP--AGRHFgRFHGEDIYTTKESERLVRLPLFYGLSPEDQRRVIATL 371
|
....
gi 1137344229 430 EEFF 433
Cdd:TIGR02379 372 CDYL 375
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
65-191 |
1.03e-13 |
|
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440205 [Multi-domain] Cd Length: 387 Bit Score: 72.09 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 65 DAFEKKLGEFIGVP----HVLTTTSGSSANLLALTALtspklgeraLKPGDEVITVAAGFPTTVNPAIQNGLIPVFVDVD 140
Cdd:COG0436 74 EAIAAYYKRRYGVDldpdEILVTNGAKEALALALLAL---------LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLD 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1137344229 141 IPT-YNIDASLIEAAVTEKSKAIMIAH----TlGNAFNLSEVRRIAD---KYNLWLIED 191
Cdd:COG0436 145 EENgFLPDPEALEAAITPRTKAIVLNSpnnpT-GAVYSREELEALAElarEHDLLVISD 202
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
63-233 |
8.50e-11 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 60.47 E-value: 8.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 63 FNDAFEKKLGEF--IGVPHVLTTTSGSSANLLALTALtspklgeraLKPGDEVITVAAGF-PTTVNPAIQNGLIPVFVDV 139
Cdd:cd01494 1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLAL---------LGPGDEVIVDANGHgSRYWVAAELAGAKPVPVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 140 DIPTYNID--ASLIEAAVTEKSKAIMIAHTL---GNAFNLSEVRRIADKYNLWLIEDCCDALGTTYEGQMVGTFGDIGTV 214
Cdd:cd01494 72 DDAGYGGLdvAILEELKAKPNVALIVITPNTtsgGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVV 151
|
170
....*....|....*....
gi 1137344229 215 SFYPAHHITMGEGGAVFTK 233
Cdd:cd01494 152 TFSLHKNLGGEGGGVVIVK 170
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
79-191 |
2.32e-10 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 62.06 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 79 HVLTTTSGSSANLLALTALtspklgeraLKPGDEVITVAAGFPTTVNPAIQNGLIPVFVDVDIPT-YNIDASLIEAAVTE 157
Cdd:PRK05764 93 QVIVTTGAKQALYNAFMAL---------LDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgFKLTVEQLEAAITP 163
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1137344229 158 KSKAIMIAH----TlGNAFNLSEVRRIAD---KYNLWLIED 191
Cdd:PRK05764 164 KTKALILNSpsnpT-GAVYSPEELEAIADvavEHDIWVLSD 203
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
26-191 |
4.60e-10 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 60.82 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 26 PFVAGTSVVPPSGKVIgaKELQLMVEASLDGWLTTGRFNDAFEKKLGEFIGVPH--------VLTTTSGSSANLLALTAL 97
Cdd:cd00609 2 DLSIGEPDFPPPPEVL--EALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGgvdvppeeIVVTNGAQEALSLLLRAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 98 tspklgeraLKPGDEVITVAAGFPTTVNPAIQNGLIPVFVDVDIP-TYNIDASLIEAAVTEKSKAIMIAH----TlGNAF 172
Cdd:cd00609 80 ---------LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEgGFLLDLELLEAAKTPKTKLLYLNNpnnpT-GAVL 149
|
170 180
....*....|....*....|..
gi 1137344229 173 NLSEVRRIAD---KYNLWLIED 191
Cdd:cd00609 150 SEEELEELAElakKHGILIISD 171
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
29-195 |
7.39e-09 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 57.26 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 29 AGTSVVPPSgkVIGAKELQLMVEASLD-------GWLTTGRFNDAfEKKLGEFIGVPH----VLTTTSGSSANLLALTAL 97
Cdd:pfam00266 6 AATTQKPQE--VLDAIQEYYTDYNGNVhrgvhtlGKEATQAYEEA-REKVAEFINAPSndeiIFTSGTTEAINLVALSLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 98 tspklgeRALKPGDEVITVAAGFPTTVNP----AIQNGLIPVFVDVDiPTYNIDASLIEAAVTEKSKAIMIAHT---LGN 170
Cdd:pfam00266 83 -------RSLKPGDEIVITEMEHHANLVPwqelAKRTGARVRVLPLD-EDGLLDLDELEKLITPKTKLVAITHVsnvTGT 154
|
170 180
....*....|....*....|....*
gi 1137344229 171 AFNLSEVRRIADKYNLWLiedCCDA 195
Cdd:pfam00266 155 IQPVPEIGKLAHQYGALV---LVDA 176
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
80-191 |
1.21e-07 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 53.59 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 80 VLTTTSGSSANLLALTALtspklgeraLKPGDEVITVAAGFPTTVNPAIQNGLIPVFVDVDIPT-YNIDASLIEAAVTEK 158
Cdd:PRK07682 84 IIVTVGASQALDVAMRAI---------INPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAK 154
|
90 100 110
....*....|....*....|....*....|....*....
gi 1137344229 159 SKAIMIAH------TLGNAFNLSEVRRIADKYNLWLIED 191
Cdd:PRK07682 155 TKAILLCSpnnptgAVLNKSELEEIAVIVEKHDLIVLSD 193
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
65-223 |
1.30e-07 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 53.08 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 65 DAFEKKLGEFIGVPHVLT--------TTSGSSANLLALTALtspklgerALKPGDEVITVAAGFPTTVNPAIQNGLIPVF 136
Cdd:pfam00155 42 PELREALAKFLGRSPVLKldreaavvFGSGAGANIEALIFL--------LANPGDAILVPAPTYASYIRIARLAGGEVVR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 137 VDV-DIPTYNIDASLIEAAVTEKSKAIMIA---HTLGNAFNLSEVRRIAD---KYNLWLIEDccDAlgttYEGQMVGTFG 209
Cdd:pfam00155 114 YPLyDSNDFHLDFDALEAALKEKPKVVLHTsphNPTGTVATLEELEKLLDlakEHNILLLVD--EA----YAGFVFGSPD 187
|
170
....*....|....*..
gi 1137344229 210 DIGTVSF---YPAHHIT 223
Cdd:pfam00155 188 AVATRALlaeGPNLLVV 204
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
66-186 |
2.85e-07 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 51.83 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 66 AFEKKLGEFIGVPHVLTTTSGSSANLLALTALTspklgeralKPGDEVITVAAG---FPTTVNPAIQNGLIPVFVDVDiP 142
Cdd:pfam01212 36 RLEDRVAELFGKEAALFVPSGTAANQLALMAHC---------QRGDEVICGEPAhihFDETGGHAELGGVQPRPLDGD-E 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1137344229 143 TYNIDASLIEAAVTE-------KSKAIMIAHTLGNAF-------NLSEVRRIADKYNL 186
Cdd:pfam01212 106 AGNMDLEDLEAAIREvgadifpPTGLISLENTHNSAGgqvvsleNLREIAALAREHGI 163
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
67-225 |
2.71e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 49.33 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 67 FEKKLGEFIGVPHVLTTTSGSSANLLALTALtspklgeraLKPGDEVITVAAGFpttvNPAIQNGLIPVFVDVDIPTY-- 144
Cdd:PRK06348 79 YSKNYDLSFKRNEIMATVGACHGMYLALQSI---------LDPGDEVIIHEPYF----TPYKDQIEMVGGKPIILETYee 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 145 ---NIDASLIEAAVTEKSKAIMI---AHTLGNAFN---LSEVRRIADKYNLWLIEDCCDALGTTYEgqmvgTFGDIGTVS 215
Cdd:PRK06348 146 dgfQINVKKLEALITSKTKAIILnspNNPTGAVFSketLEEIAKIAIEYDLFIISDEVYDGFSFYE-----DFVPMATLA 220
|
170
....*....|
gi 1137344229 216 FYPAHHITMG 225
Cdd:PRK06348 221 GMPERTITFG 230
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
69-191 |
2.94e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 49.08 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 69 KKLGEFIGVPHVLTTTSGSSANLLALTALTSPklgeralkpGDEVI------TVAAGFPTTVNPAIqnglipvfvdVDIP 142
Cdd:PRK07568 80 KKWGIDVEPDEILITNGGSEAILFAMMAICDP---------GDEILvpepfyANYNGFATSAGVKI----------VPVT 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1137344229 143 TY--------NIDAslIEAAVTEKSKAIMIAH----TlGNAFNLSEVRRIAD---KYNLWLIED 191
Cdd:PRK07568 141 TKieegfhlpSKEE--IEKLITPKTKAILISNpgnpT-GVVYTKEELEMLAEiakKHDLFLISD 201
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
107-164 |
3.53e-06 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 49.04 E-value: 3.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1137344229 107 LKPGDEVITVAAGFPTtVNPAIQN-GLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMI 164
Cdd:PRK06836 117 LNPGDEVIVFAPYFVE-YRFYVDNhGGKLVVVPTDTDTFQPDLDALEAAITPKTKAVII 174
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
60-193 |
7.01e-06 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 48.20 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 60 TGRFNDAFE---KKLGEFIGVPH----VLTTTSGSSANLLALTaltspkLGERALKPGDEVITVAAGFPTTVNP----AI 128
Cdd:PLN02855 71 SAKATDAYElarKKVAAFINASTsreiVFTRNATEAINLVAYT------WGLANLKPGDEVILSVAEHHSNIVPwqlvAQ 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1137344229 129 QNGLIPVFVDVDiPTYNIDASLIEAAVTEKSKAIMIAH---TLGNAFNLSEVRRIADKYNLWLIEDCC 193
Cdd:PLN02855 145 KTGAVLKFVGLT-PDEVLDVEQLKELLSEKTKLVATHHvsnVLGSILPVEDIVHWAHAVGAKVLVDAC 211
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
72-191 |
7.36e-05 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 44.55 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 72 GEFIGVPHVLTTTSGSSANLLALTALTSpklgeralkPGDEVITVAAGFPTTVNPAIQNGLIPVFVDVDIPT--YNIDAS 149
Cdd:PRK06108 79 GVATPPERIAVTSSGVQALMLAAQALVG---------PGDEVVAVTPLWPNLVAAPKILGARVVCVPLDFGGggWTLDLD 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1137344229 150 LIEAAVTEKSKAIMIahtlgNAFN-----------LSEVRRIADKYNLWLIED 191
Cdd:PRK06108 150 RLLAAITPRTRALFI-----NSPNnptgwtasrddLRAILAHCRRHGLWIVAD 197
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
107-191 |
7.89e-05 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 44.71 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 107 LKPGDEVITVAAGFPTtVNPAIQ-NGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAIMIAH---TLGNAFNLSEVRRIA- 181
Cdd:PRK07683 110 LEPGTEVILPAPIYPG-YEPIIRlCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVVLPYpsnPTGVTLSKEELQDIAd 188
|
90
....*....|...
gi 1137344229 182 ---DKyNLWLIED 191
Cdd:PRK07683 189 vlkDK-NIFVLSD 200
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
65-182 |
1.13e-04 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 44.12 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 65 DAFEKKLGEFIGVPHVLTTTSGSSANLLALTALtspklgeraLKPGDEVITVAAGFPTTVNPA---IQNGLIPV-FVDVD 140
Cdd:cd00614 43 DALEKKLAALEGGEAALAFSSGMAAISTVLLAL---------LKAGDHVVASDDLYGGTYRLFerlLPKLGIEVtFVDPD 113
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1137344229 141 IPtynidaSLIEAAVTEKSKAIMIaHTLGN-AFNLSEVRRIAD 182
Cdd:cd00614 114 DP------EALEAAIKPETKLVYV-ESPTNpTLKVVDIEAIAE 149
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
65-197 |
1.66e-04 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 43.59 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 65 DAFE---KKLGEFIGV--PHVLTTTSGSSA--NLLALTaltspkLGEraLKPGDEVITVAAGFPTTVNP----AIQNGLI 133
Cdd:COG0520 59 DAYEaarEKVARFIGAasPDEIIFTRGTTEaiNLVAYG------LGR--LKPGDEILITEMEHHSNIVPwqelAERTGAE 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1137344229 134 PVFVDVDiPTYNIDASLIEAAVTEKSKAIMIAH---TLGNAFNLSEVRRIADKYNLWLIEDCCDALG 197
Cdd:COG0520 131 VRVIPLD-EDGELDLEALEALLTPRTKLVAVTHvsnVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
81-200 |
2.22e-04 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 43.16 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 81 LTTTSGSSANLLALTALtspklgeraLKPGDEVITVAAGFPTTVNP---AIQN-GLIPVFVDVDiptyniDASLIEAAVT 156
Cdd:PRK05994 82 LAVASGHAAQFLVFHTL---------LQPGDEFIAARKLYGGSINQfghAFKSfGWQVRWADAD------DPASFERAIT 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1137344229 157 EKSKAIMI---AHTLGNAFNLSEVRRIADKYNLWLIEDccDALGTTY 200
Cdd:PRK05994 147 PRTKAIFIesiANPGGTVTDIAAIAEVAHRAGLPLIVD--NTLASPY 191
|
|
| PRK08247 |
PRK08247 |
methionine biosynthesis PLP-dependent protein; |
130-191 |
3.01e-04 |
|
methionine biosynthesis PLP-dependent protein;
Pssm-ID: 181320 [Multi-domain] Cd Length: 366 Bit Score: 42.77 E-value: 3.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1137344229 130 NGLIPVFVDvdipTYNIDAslIEAAVTEKSKAIMI---AHTLGNAFNLSEVRRIADKYNLWLIED 191
Cdd:PRK08247 114 WNVRFVYVN----TASLKA--IEQAITPNTKAIFIetpTNPLMQETDIAAIAKIAKKHGLLLIVD 172
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
82-193 |
6.67e-04 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 41.42 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 82 TTTSGSS-ANLLALTALTSPKLGERALKPGDEVITVAAGFPTTVNPAIQ-NGLI----PVFVDVDiPTYNIDASLIEAAV 155
Cdd:cd06450 61 VFTSGGSeSNLLALLAARDRARKRLKAGGGRGIDKLVIVCSDQAHVSVEkAAAYldvkVRLVPVD-EDGRMDPEALEAAI 139
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1137344229 156 TEKSKA----IMIAHTLGN----AF-NLSEVRRIADKYNLWLIEDCC 193
Cdd:cd06450 140 DEDKAEglnpIMVVATAGTtdtgAIdPLEEIADLAEKYDLWLHVDAA 186
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
69-207 |
1.06e-03 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 40.95 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 69 KKLGEFIGVPHVLTTTSGSSANLLALTALtspklgeraLKPGDEVITVAAGFPTTVNPAIQNGLIPVFVD-VDIPTYNID 147
Cdd:PRK08363 85 RKNGVDITPDDVRVTAAVTEALQLIFGAL---------LDPGDEILIPGPSYPPYTGLVKFYGGVPVEYRtIEEEGWQPD 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1137344229 148 ASLIEAAVTEKSKAIMIAH------TLGNAFNLSEVRRIADKYNLWLIED-CCDALgtTYEGQMVGT 207
Cdd:PRK08363 156 IDDIRKKITEKTKAIAVINpnnptgALYEKKTLKEILDIAGEHDLPVISDeIYDLM--TYEGKHVSP 220
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
82-164 |
1.50e-03 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 40.67 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 82 TTTSGSSANLL-ALTALtspklgeraLKPGDEVITVAAGFPTTVnPAIQ-NGLIPVFVDVDIPTYNIDASLIEAAVTEKS 159
Cdd:PRK09082 95 TVTAGATEALFaAILAL---------VRPGDEVIVFDPSYDSYA-PAIElAGGRAVRVALQPPDFRVDWQRFAAAISPRT 164
|
....*
gi 1137344229 160 KAIMI 164
Cdd:PRK09082 165 RLIIL 169
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
80-191 |
2.63e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 39.67 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 80 VLTTTSGSSANLLALTALTSPklgeralkpGDEVITVAagfPTTVNP--AIQ-NGLIPVFVDVDiPTYNIDASLIEAAVT 156
Cdd:PRK05957 92 IVVTAGSNMAFMNAILAITDP---------GDEIILNT---PYYFNHemAITmAGCQPILVPTD-DNYQLQPEAIEQAIT 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1137344229 157 EKSKAIMiahTL------GNAF---NLSEVRRIADKYNLWLIED 191
Cdd:PRK05957 159 PKTRAIV---TIspnnptGVVYpeaLLRAVNQICAEHGIYHISD 199
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
83-188 |
3.40e-03 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 439846 [Multi-domain] Cd Length: 460 Bit Score: 39.43 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 83 TTSGSSANLLALTAL---TSPKLGERALKPGDEVITVAAgfPTTVNPAIQ----------NGLIPVFVDvdiPTYNIDAS 149
Cdd:COG0076 131 TSGGTEANLLALLAArdrALARRVRAEGLPGAPRPRIVV--SEEAHSSVDkaarllglgrDALRKVPVD---EDGRMDPD 205
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1137344229 150 LIEAAVTEKSKA----IMIAHTLGN----AF-NLSEVRRIADKYNLWL 188
Cdd:COG0076 206 ALEAAIDEDRAAglnpIAVVATAGTtntgAIdPLAEIADIAREHGLWL 253
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
84-164 |
5.22e-03 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 38.80 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344229 84 TSGssanllALTALTSPKLGerALKPGDEVITVAAGFPTTVnPAI-QNGLIPVFVDVDIPTYNIDASLIEAAVTEKSKAI 162
Cdd:PRK08912 93 TSG------ATEALAAALLA--LVEPGDEVVLFQPLYDAYL-PLIrRAGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAV 163
|
..
gi 1137344229 163 MI 164
Cdd:PRK08912 164 LL 165
|
|
| |
